The kinetic parameters, KM and kcat of the hydrolysis of L-asparagine by nitrotyrosyl-asparaginase have been determined over a wide pH range of 4.50–8.85. It has been shown that the modification of the asparaginase leads to a marked increase in the Michaelis constant and to an insignificant change in kcat. A hypothesis has been put forward concerning the possible participation of the hydroxy group of the tyrosine residue in the formation of the enzyme-substrate complex.
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Milman, I.A., Geiman, I.I., Pinka, U.A. et al. pH Dependence of the kinetic parameters of nitrotyrosyl-asparaginase. Chem Nat Compd 14, 302–304 (1978). https://doi.org/10.1007/BF00713321
- Organic Chemistry
- Kinetic Parameter
- Hydroxy Group
- Tyrosine Residue